Complex formation between AmtB and GlnK: an ancestral role in prokaryotic nitrogen control

A Javelle, M Merrick

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

Ammonium transport proteins belonging to the Amt family are ubiquitous in prokaryotes. In Escherichia coli, the AmtB protein and the associated P(II) signal transduction protein (GlnK) have recently been recognized as an ammonium sensory system that effectively couples the intracellular nitrogen regulation (Ntr) system to external changes in ammonium availability. Given the almost invariant coupling of AmtB and GlnK in bacteria and archaea it seems probable that these two proteins may constitute an ancestral nitrogen-responsive system that has been coupled with a variety of unrelated nitrogen regulatory processes, which are now found in prokaryotes. The multiplicity of P(II) proteins could therefore be considered to have evolved from an ancestral GlnK-like protein and to have subsequently been adapted to control many other aspects of nitrogen metabolism.

LanguageEnglish
Pages170-172
Number of pages3
JournalBiochemical Society Transactions
Volume33
Issue numberPt 1
DOIs
Publication statusPublished - 1 Feb 2005

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Nitrogen
Ammonium Compounds
Proteins
Signal transduction
Archaea
Metabolism
Escherichia coli
Signal Transduction
Bacteria
Carrier Proteins
Availability

Keywords

  • bacteria
  • bacterial proteins
  • cation transport proteins
  • Escherichia coli proteins
  • nitrogen alloying
  • operon

Cite this

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Complex formation between AmtB and GlnK : an ancestral role in prokaryotic nitrogen control. / Javelle, A; Merrick, M.

In: Biochemical Society Transactions, Vol. 33, No. Pt 1, 01.02.2005, p. 170-172.

Research output: Contribution to journalArticle

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T2 - Biochemical Society Transactions

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AU - Merrick, M

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AB - Ammonium transport proteins belonging to the Amt family are ubiquitous in prokaryotes. In Escherichia coli, the AmtB protein and the associated P(II) signal transduction protein (GlnK) have recently been recognized as an ammonium sensory system that effectively couples the intracellular nitrogen regulation (Ntr) system to external changes in ammonium availability. Given the almost invariant coupling of AmtB and GlnK in bacteria and archaea it seems probable that these two proteins may constitute an ancestral nitrogen-responsive system that has been coupled with a variety of unrelated nitrogen regulatory processes, which are now found in prokaryotes. The multiplicity of P(II) proteins could therefore be considered to have evolved from an ancestral GlnK-like protein and to have subsequently been adapted to control many other aspects of nitrogen metabolism.

KW - bacteria

KW - bacterial proteins

KW - cation transport proteins

KW - Escherichia coli proteins

KW - nitrogen alloying

KW - operon

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